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Both Tel monomers and oligomers are efficiently sumoylated on K11 in vitro; but in cells only Tel oligomers are found conjugated with SUMO, whereas sumoylation of Tel monomers is transitory and appears to sensitize them for proteasomal degradation.Mechanistically, sumoylation of K11 inhibits repression of gene expression by full-length Tel.Cell proliferation and differentiation are governed by a finely controlled balance between repression and activation of gene expression.The vertebrate Ets transcriptional repressor Tel (ETV6) and its invertebrate orthologue Yan, play pivotal roles in cell fate determination although the precise mechanisms by which repression of gene expression by these factors is achieved are not clearly defined.The mobile phases consisted of 0.04% formic acid-0.4% acetonitrile (phase A) and 0.04% formic acid-90% acetonitrile (phase B).A 45-min linear gradient from 0 to 60% mobile phase B was used at a flow rate of 0.2 μl/min.However, the exact nature of repression by Tel/Yan is incompletely defined.
Deciphering the precise mechanisms of action of Yan/Tel is important for understanding the control of progenitor cell differentiation and tissue patterning.
In accordance with this observation, we found that sumoylation impedes Tel association with DNA.
By contrast, a Tel isoform lacking K11 (Tel M43) is strongly repressive.
MALDI-TOF analyses were performed on an Ultraflex II time-of-flight mass spectrometer (Bruker Daltonics, Bremen, Germany) controlled by the Flexcontrol, version 2.0, software package.
For liquid chromatography-mass spectrometry (LC-MS) analysis, samples were injected onto a capillary high-performance LC system (Ultimate; Dionex, Amsterdam, The Netherlands) equipped with a peptide trap column (Pepmap 100; 0.3-mm internal diameter by 1 mm; Dionex, Amsterdam, The Netherlands) and an analytical column (Pepmap; 0.075 by 150 mm; Dionex, Amsterdam, The Netherlands).